1e0k: Difference between revisions
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|LIGAND= | |LIGAND= | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GENE 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | |GENE= GENE 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 Enterobacteria phage T7]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0k OCA], [http://www.ebi.ac.uk/pdbsum/1e0k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0k RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
1E0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 1E0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t7 Enterobacteria phage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0K OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10892646 10892646] | Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10892646 10892646] | ||
[[Category: | [[Category: Enterobacteria phage t7]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ellenberger, T.]] | [[Category: Ellenberger, T.]] | ||
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[[Category: helicase]] | [[Category: helicase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:41 2008'' | ||
Revision as of 19:52, 30 March 2008
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GENE 4 (Enterobacteria phage T7) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GP4D HELICASE FROM PHAGE T7
OverviewOverview
We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation.
About this StructureAbout this Structure
1E0K is a Single protein structure of sequence from Enterobacteria phage t7. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:10892646
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